Sahlan Muhamad, Zako Tamotsu, Yohda Masafumi
Department of Chemical Engineering, Universitas Indonesia, Depok, Indonesia.
Research Centre for Biomedical Engineering, Faculty of Engineering, Universitas Indonesia, Depok, Indonesia.
Biophys Rev. 2018 Apr;10(2):339-345. doi: 10.1007/s12551-018-0400-0. Epub 2018 Feb 9.
Prefoldin is a hexameric molecular chaperone found in the cytosol of archaea and eukaryotes. Its hexameric complex is built from two related classes of subunits and has the appearance of a jellyfish: its body consists of a double beta-barrel assembly with six long tentacle-like coiled coils protruding from it. Using the tentacles, prefoldin captures an unfolded protein substrate and transfers it to a group II chaperonin. The prefoldin-group II chaperonin system is thought to be important for the folding of newly synthesized proteins and for their maintenance, or proteostasis, in the cytosol. Based on structural information of archaeal prefoldins, the mechanisms of substrate recognition and prefoldin-chaperonin cooperation have been investigated. In contrast, the role and mechanism of eukaryotic PFDs remain unknown. Recent studies have shown that prefoldin plays an important role in proteostasis and is involved in various diseases. In this paper, we review a series of studies on the molecular mechanisms of archaeal prefoldins and introduce recent findings about eukaryotic prefoldin.
前折叠素是一种六聚体分子伴侣，存在于古细菌和真核生物的细胞质中。其六聚体复合物由两类相关的亚基组成，外观像水母：它的主体由一个双β桶组件构成，有六条长长的触手状卷曲螺旋从主体伸出。前折叠素利用这些触手捕获未折叠的蛋白质底物，并将其转移给Ⅱ型伴侣蛋白。前折叠素 - Ⅱ型伴侣蛋白系统被认为对新合成蛋白质的折叠以及它们在细胞质中的维持（即蛋白质稳态）很重要。基于古细菌前折叠素的结构信息，人们研究了底物识别和前折叠素 - 伴侣蛋白合作的机制。相比之下，真核生物前折叠素的作用和机制仍然未知。最近的研究表明，前折叠素在蛋白质稳态中起重要作用，并与多种疾病有关。在本文中，我们综述了一系列关于古细菌前折叠素分子机制的研究，并介绍了关于真核生物前折叠素的最新发现。
